4F3X
Crystal structure of putative aldehyde dehydrogenase from Sinorhizobium meliloti 1021 complexed with NAD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004030 | molecular_function | aldehyde dehydrogenase [NAD(P)+] activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004030 | molecular_function | aldehyde dehydrogenase [NAD(P)+] activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004030 | molecular_function | aldehyde dehydrogenase [NAD(P)+] activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004030 | molecular_function | aldehyde dehydrogenase [NAD(P)+] activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAD A 500 |
| Chain | Residue |
| A | ILE145 |
| A | ASN209 |
| A | ILE212 |
| A | ILE222 |
| A | THR223 |
| A | GLY224 |
| A | ASP225 |
| A | THR228 |
| A | LYS231 |
| A | GLY248 |
| A | CYS280 |
| A | ALA146 |
| A | GLN327 |
| A | ARG330 |
| A | GLU378 |
| A | PHE380 |
| A | PRO147 |
| A | TRP148 |
| A | LYS172 |
| A | SER174 |
| A | GLU175 |
| A | GLY204 |
| A | GLY208 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 501 |
| Chain | Residue |
| A | ASN65 |
| A | LYS69 |
| A | ASP72 |
| A | HOH749 |
| D | GLU75 |
| D | ARG109 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 501 |
| Chain | Residue |
| A | ILE139 |
| B | GLN426 |
| B | HOH682 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAD B 502 |
| Chain | Residue |
| B | ILE145 |
| B | ALA146 |
| B | PRO147 |
| B | TRP148 |
| B | LYS172 |
| B | SER174 |
| B | GLU175 |
| B | GLY204 |
| B | GLY208 |
| B | ASN209 |
| B | ILE222 |
| B | THR223 |
| B | GLY224 |
| B | ASP225 |
| B | THR228 |
| B | LYS231 |
| B | LEU247 |
| B | GLY248 |
| B | CYS280 |
| B | GLN327 |
| B | GLU378 |
| B | PHE380 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 503 |
| Chain | Residue |
| B | ASN65 |
| B | LYS69 |
| B | HOH672 |
| site_id | AC6 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAD C 500 |
| Chain | Residue |
| C | ILE145 |
| C | ALA146 |
| C | PRO147 |
| C | TRP148 |
| C | LYS172 |
| C | SER174 |
| C | GLU175 |
| C | GLY204 |
| C | GLY208 |
| C | ASN209 |
| C | ILE212 |
| C | ILE222 |
| C | THR223 |
| C | GLY224 |
| C | ASP225 |
| C | THR228 |
| C | LYS231 |
| C | CYS280 |
| C | GLN327 |
| C | ARG330 |
| C | GLU378 |
| C | PHE380 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL C 501 |
| Chain | Residue |
| B | ARG109 |
| C | ASN65 |
| C | LYS69 |
| site_id | AC8 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD D 500 |
| Chain | Residue |
| D | THR228 |
| D | LYS231 |
| D | GLY248 |
| D | CYS280 |
| D | GLN327 |
| D | ARG330 |
| D | GLU378 |
| D | PHE380 |
| D | HOH675 |
| D | ILE145 |
| D | ALA146 |
| D | PRO147 |
| D | TRP148 |
| D | ASN149 |
| D | LYS172 |
| D | SER174 |
| D | GLU175 |
| D | GLY204 |
| D | GLU205 |
| D | GLY208 |
| D | ASN209 |
| D | ILE212 |
| D | ILE222 |
| D | THR223 |
| D | GLY224 |
| D | ASP225 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL D 501 |
| Chain | Residue |
| A | ARG109 |
| D | ASN65 |
| D | LEU68 |
| D | LYS69 |
| D | ASP72 |
Functional Information from PROSITE/UniProt
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKAP |
| Chain | Residue | Details |
| A | LEU245-PRO252 |
